The position of hydrophobic residues tunes peptide self-assembly.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 24995505.
- Also identified by DOI 10.1039/c4sm01065e.
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Abstract
The final structure and properties of synthetic peptides mainly depend on their sequence composition and experimental conditions. This work demonstrates that a variation in the positions of hydrophobic residues within a peptide sequence can tune the self-assembly. Techniques employed are atomic force microscopy, transmission electron microscopy and an innovative method based on surface acoustic waves. In addition, a systematic investigation on pH dependence was carried out by utilizing constant experimental parameters.
Medical subject headings
- Amino Acids
- Hydrophobic and Hydrophilic Interactions
- Peptides
- Protein Structure, Secondary